ID   A0A1Y2DAE8_9PEZI        Unreviewed;       607 AA.
AC   A0A1Y2DAE8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=BCR38DRAFT_356106 {ECO:0000313|EMBL:ORY56167.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY56167.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY56167.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY56167.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORY56167.1}.
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DR   EMBL; MCFJ01000024; ORY56167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2DAE8; -.
DR   STRING; 1141098.A0A1Y2DAE8; -.
DR   InParanoid; A0A1Y2DAE8; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF80; -; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..607
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012124120"
FT   DOMAIN          344..358
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          225..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         140..143
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   607 AA;  65402 MW;  BEC3236B05CED14C CRC64;
     MLRHAFVSFL LTATGVAAQN STTSYDYVVV GSGPGGAPLA ANLARAGHSV LLLEAGDDQA
     NNPNISQIAN FNPAASDETT RWDFWTKHSD DPERELKYEH MVWRQKDGSF YTGLDPPAGA
     EQLGIWYPRT GTLGGCAMHN GGVCSLPSDD DWNDIAKLTG DKSWKAENMR KHFVKLEKNE
     YLEPGAPGHG FDGWVSTILA GTDWATEDVD VTTIMKKIVN ATGGDPSQLP ELAKKDVNAP
     DPNRDQDTGV NGMAIHATSQ GLRSGTNSYL KATLADAAKY PLTIQLESLA TKILFSKGTA
     EPKAIGVEYL KGKSLYSGDP RYKASAKGPV GQVFAKKEVI IAGGAFNSPQ ILKLSGIGPA
     AELKKFNIPV VKDLPGVGEN LADNYEGYVL GLADKPLTGL SMTSVSVFLK TPTAPKHRNI
     HAWCGPLSFE GFWPGFPHEY GPTEWECPFV HMNPRSQAGY VHLKSADPRD TPDINLKFFE
     TGEDKDLTEM LDAVKTFRKA FQSVTAPIGP FDELHPCPGK NQDCSDAAIK ETLKLQAHSH
     HATSTCAIGA ADDEMAVLDS EFRVRGVKNL RVVDASAFPK VPGAFPVCPT FMISEKASEV
     ILAAAKA
//